2bpt
From Proteopedia
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| - | [[Image:2bpt.gif|left|200px]] | + | [[Image:2bpt.gif|left|200px]] |
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| - | '''STRUCTURE OF THE NUP1P:KAP95P COMPLEX''' | + | {{Structure |
| + | |PDB= 2bpt |SIZE=350|CAPTION= <scene name='initialview01'>2bpt</scene>, resolution 1.99Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''STRUCTURE OF THE NUP1P:KAP95P COMPLEX''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2BPT is a [ | + | 2BPT is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. The following page contains interesting information on the relation of 2BPT with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb85_1.html Importins]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BPT OCA]. |
==Reference== | ==Reference== | ||
| - | Structural basis for the high-affinity binding of nucleoporin Nup1p to the Saccharomyces cerevisiae importin-beta homologue, Kap95p., Liu SM, Stewart M, J Mol Biol. 2005 Jun 10;349(3):515-25. Epub 2005 Apr 19. PMID:[http:// | + | Structural basis for the high-affinity binding of nucleoporin Nup1p to the Saccharomyces cerevisiae importin-beta homologue, Kap95p., Liu SM, Stewart M, J Mol Biol. 2005 Jun 10;349(3):515-25. Epub 2005 Apr 19. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15878174 15878174] |
[[Category: Importins]] | [[Category: Importins]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: nucleoporin]] | [[Category: nucleoporin]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:05:07 2008'' |
Revision as of 14:05, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE OF THE NUP1P:KAP95P COMPLEX
Overview
Macromolecules are transported across the nuclear envelope most frequently by karyopherin/importin-beta superfamily members that are constructed from HEAT repeats. Transport of Kap95p (yeast importin-beta), the principal carrier for protein import, through nuclear pore complexes is facilitated by interactions with nucleoporins containing FG repeats. However, Nup1p interacts more strongly with Kap95p than other FG-nucleoporins. To establish the basis of this increased affinity, we determined the structure of Kap95p complexed with Nup1p residues 963-1076 that contain the high-affinity Kap95p binding site. Nup1p binds Kap95p at three sites between the outer A-helices of HEAT repeats 5, 6, 7 and 8. At each site, phenylalanine residues from Nup1p are buried in hydrophobic depressions between adjacent HEAT repeats. Although the Nup1p and generic FG-nucleoporin binding sites on Kap95p overlap, Nup1p binding differs markedly and has contributions from additional hydrophobic residues, together with interactions generated by the intimate contact of the linker between Nup1 residues 977-987 with Kap95p. The length and composition of this linker is crucial and suggests how differences in affinity for Kap95p both between and within FG-nucleoporins arise.
About this Structure
2BPT is a Protein complex structure of sequences from Saccharomyces cerevisiae. The following page contains interesting information on the relation of 2BPT with [Importins]. Full crystallographic information is available from OCA.
Reference
Structural basis for the high-affinity binding of nucleoporin Nup1p to the Saccharomyces cerevisiae importin-beta homologue, Kap95p., Liu SM, Stewart M, J Mol Biol. 2005 Jun 10;349(3):515-25. Epub 2005 Apr 19. PMID:15878174
Page seeded by OCA on Thu Mar 20 16:05:07 2008
